ID A0A1B9H971_9TREE Unreviewed; 642 AA. AC A0A1B9H971; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 12-AUG-2020, entry version 20. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=I317_06377 {ECO:0000313|EMBL:OCF39825.1}; OS Kwoniella heveanensis CBS 569. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Kwoniella. OX NCBI_TaxID=1296119 {ECO:0000313|EMBL:OCF39825.1, ECO:0000313|Proteomes:UP000092564}; RN [1] {ECO:0000313|EMBL:OCF39825.1, ECO:0000313|Proteomes:UP000092564} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 569 {ECO:0000313|EMBL:OCF39825.1, RC ECO:0000313|Proteomes:UP000092564}; RG The Broad Institute Genome Sequencing Platform; RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D., RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Cryptococcus heveanensis CBS569."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000092564} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 569 {ECO:0000313|Proteomes:UP000092564}; RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D., RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.; RT "Evolution of pathogenesis and genome organization in the Tremellales."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10- CC methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH; CC Xref=Rhea:RHEA:19821, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, CC ChEBI:CHEBI:18608, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.20; CC Evidence={ECO:0000256|ARBA:ARBA00001287, CC ECO:0000256|RuleBase:RU003862}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10- CC methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH; CC Xref=Rhea:RHEA:19817, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, CC ChEBI:CHEBI:18608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.20; CC Evidence={ECO:0000256|ARBA:ARBA00000431, CC ECO:0000256|RuleBase:RU003862}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU004254}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family. CC {ECO:0000256|ARBA:ARBA00006743, ECO:0000256|RuleBase:RU003862}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KV700245; OCF39825.1; -; Genomic_DNA. DR EnsemblFungi; OCF39825; OCF39825; I317_06377. DR OrthoDB; 338303at2759; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000092564; Unassembled WGS sequence. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR CDD; cd00537; MTHFR; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR004621; Fadh2_euk. DR InterPro; IPR003171; Mehydrof_redctse. DR Pfam; PF02219; MTHFR; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR TIGRFAMs; TIGR00677; fadh2_euk; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU003862}. FT REGION 325..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 364..396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 327..345 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 642 AA; 70995 MW; 3487D7E436434105 CRC64; MTQLTSLISS HDGPFHTFEF FPPRTEAGLV NLLDRIGRLA AAPMPAPLAV SVTWGAGGST ADKSLELAEQ VVKLGVEVIL HLTCTNMAKE KVDQALEKCR SLGITNILAL RGDPPRSEEY AVDPNPQPDF FQHADDLVRY IRKEYGDYFC IGVAGYPTPH SDSESAESDL HYLKVKCDAG ADYIITQLFY DVEGFLEWVT TCRERGITQP IIPGIMPIQN FSSFRRLVNL TKCPVPESIM ADLQPISSDD AAVKRYGAEL ATRMVRQVFQ SGLVPGVHFC TLNLEKSVRT ILENLGWSAT SDPNLRASPF IRYNRLIEDD EPQTNGAIAI NGHSDGSPKN QVKDLSISPS EASVLAQWGL THHAPPPVPK RGLGTQGGPG GITGASGEDS WDEYPNGRFT DVRSPAYGEI DGWGSGLKIT AAQALKEWGT PTNVNELAKF FVSYLESSPS TPTTPFCDLP LSSESIPILP HLIALNSEKI QHWTVGSQPA VDAANSEDPV FGWGPRGGYV FQKAFVEFFV REEEVKRLEE KVEKKGNGLI SMYAGNKKGD FRTNTEKDAV NAVTWGVFPG QEIVQSTIIE AESFHAWKEE AFDIWTEWSL LYPRLSPSRR LLESIAGEWW LVSLIHHDYK DPDALWKFLL EE //